atpH:Gene Product(s)
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| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| Nomenclature | Function | Interactions | Localization | Sequence | Structure | Resources | Accessions | Links | References | Suggestions |
Nomenclature
| Standard name |
AtpH product |
|---|---|
| Synonyms |
F1 sector of membrane-bound ATP synthase, delta subunit product[1], B3735 product[2][1], Unc product[2][1], UncH product[2][1], PapE product[2][1], AtpH product[2][1] |
| Product description |
ATP synthase, F1 complex, δ subunit[2][3]; Component of ; ATP synthase, F1 complex[2][3]; ATP synthase[2][3] |
| EC number (for enzymes) | |
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Notes
Function
Gene Ontology
| Qualifier | GO ID | GO term name | Reference(s) | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0005737 |
cytoplasm |
C |
Seeded from EcoCyc 11.1[3]. |
required fields missing | ||||
| GO:0015986 |
ATP synthesis coupled proton transport |
IMP: Inferred from Mutant Phenotype |
P |
Seeded from EcoCyc 11.1[3]. |
complete | |||
|
Contributes to |
GO:0046933 |
hydrogen ion transporting ATP synthase activity, rotational mechanism |
IDA: Inferred from Direct Assay |
F |
complete | |||
| GO:0045261 |
proton-transporting ATP synthase complex, catalytic core F(1) |
IMP: Inferred from Mutant Phenotype |
C |
Component of F1 complex, with gene products of uncA (alpha), uncD (beta), uncG (gamma) and uncC (epsilon) - for review see Chap 19 of Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd Edition. |
complete | |||
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Interactions
| Partner Type | Partner | Notes |
|---|---|---|
|
Protein |
Subunits of ATP synthase, F1 complex |
could be indirect |
|
Protein |
Subunits of ATP synthase |
could be indirect |
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Notes
Localization
| Compartment | Description | Evidence | Notes |
|---|---|---|---|
|
plasma membrane |
From EcoCyc[3] | ||
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Notes
Structure and Physical Properties
Physical Properties
| Sequence |
MSEFITVARP YAKAAFDFAV EHQSVERWQD MLAFAAEVTK NEQMAELLSG ALAPETLAES FIAVCGEQLD ENGQNLIRVM AENGRLNALP DVLEQFIHLR AVSEATAEVD VISAAALSEQ QLAKISAAME KRLSRKVKLN CKIDKSVMAG VIIRAGDMVI DGSVRGRLER LADVLQS |
|---|---|
| Mol. Wt |
19.33 kDa (calc) [2] |
| pI |
5.11[2] |
| Extinction coefficient |
6990 - 7240 (calc based on 1 Y, 1 W, and 2 C residues) |
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Domains/Motifs/Modification Sites
| Type | Residues | Description | Notes |
|---|---|---|---|
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Structure
| Structure Type | Organism | Accession | Residues covered | Notes |
|---|---|---|---|---|
|
NMR, MINIMIZED AVERAGE STRUCTURE |
Escherichia coli |
1ABV N-TERMINAL DOMAIN OF THE DELTA SUBUNIT OF THE F1F0-ATP SYNTHASE FROM ESCHERICHIA COLI, NMR, MINIMIZED AVERAGE STRUCTURE |
||
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Notes
Gene Product Resources
| Resource type | Source | Notes/Reference |
|---|---|---|
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Notes
Accessions in Other Databases
| Database | Accession | Notes |
|---|---|---|
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Notes
Links
| Name | URL | Comments |
|---|---|---|
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References
See Help:References for how to manage references in EcoliWiki.
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 3.0 3.1 3.2 3.3 3.4 3.5 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 4.0 4.1 Humbert, R et al. (1983) Escherichia coli mutants defective in the uncH gene. J. Bacteriol. 153 416-22 PubMed
- ↑ Klionsky, DJ & Simoni, RD (1985) Assembly of a functional F1 of the proton-translocating ATPase of Escherichia coli. J. Biol. Chem. 260 11200-6 PubMed
Categories
- GO:0005737 ! cytoplasm
- GO:0015986 ! ATP synthesis coupled proton transport
- GO:0046933 ! hydrogen ion transporting ATP synthase activity, rotational mechanism
- GO:0045261 ! proton-transporting ATP synthase complex, catalytic core F(1)
- Proteins
- GO:0016471 ! vacuolar proton-transporting V-type ATPase complex
- Complex:ATP synthase, F1 complex
- Complex:ATP synthase
- Location:cytoplasm
- Location:plasma membrane
- Products with structures in PDB